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Title: Synthesis of the low molecular weight heat shock proteins in plants

Abstract

Heat shock of living tissue induces the synthesis of a unique group of proteins, the heat shock proteins. In plants, the major group of heat shock proteins has a molecular mass of 15 to 25 kilodaltons. Accumulation to these proteins to stainable levels has been reported in only a few species. To examine accumulation of the low molecular weight heat shock proteins in a broader range of species, two-dimensional electrophoresis was used to resolve total protein from the following species: soybean (Glycine max L. Merr., var Wayne), pea (Pisum sativum L., var Early Alaska), sunflower (Helianthus annuus L.), wheat (Triticum asetivum L.), rice (Oryza sativa L., cv IR-36), maize (Zea mays L.), pearl millet (Pennisetum americanum L. Leeke, line 23DB), and Panicum miliaceum L. When identified by both silver staining and incorporation of radiolabel, a diverse array of low molecular weight heat shock proteins was synthesized in each of these species. These proteins accumulated to significant levels after three hours of heat shock but exhibited considerable heterogeneity in isoelectric point, molecular weight, stainability, and radiolabel incorporation. Although most appeared to be synthesized only during heat shock, some were detectable at low levels in control tissue. Compared to the monocots, amore » higher proportion of low molecular weight heat shock proteins was detectable in control tissues from dicots.« less

Authors:
;  [1]
  1. (Univ., of Georgia, Athens (USA))
Publication Date:
OSTI Identifier:
7098837
DOE Contract Number:  
AS09-80ER10678
Resource Type:
Journal Article
Resource Relation:
Journal Name: Plant Physiology; (USA); Journal Volume: 84:4
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; 59 BASIC BIOLOGICAL SCIENCES; PLANTS; TEMPERATURE EFFECTS; PROTEINS; BIOSYNTHESIS; GLYCINE HISPIDA; HYPERTHERMIA; MAIZE; MILLET; PISUM; RICE; SUNFLOWERS; TRACER TECHNIQUES; TRITIUM COMPOUNDS; WHEAT; BODY TEMPERATURE; CEREALS; GRASS; HYDROGEN COMPOUNDS; ISOTOPE APPLICATIONS; LEGUMINOSAE; LILIOPSIDA; MAGNOLIOPHYTA; MAGNOLIOPSIDA; ORGANIC COMPOUNDS; SYNTHESIS; 560200* - Thermal Effects; 550201 - Biochemistry- Tracer Techniques

Citation Formats

Mansfield, M.A., and Key, J.L. Synthesis of the low molecular weight heat shock proteins in plants. United States: N. p., 1987. Web. doi:10.1104/pp.84.4.1007.
Mansfield, M.A., & Key, J.L. Synthesis of the low molecular weight heat shock proteins in plants. United States. doi:10.1104/pp.84.4.1007.
Mansfield, M.A., and Key, J.L. Sat . "Synthesis of the low molecular weight heat shock proteins in plants". United States. doi:10.1104/pp.84.4.1007.
@article{osti_7098837,
title = {Synthesis of the low molecular weight heat shock proteins in plants},
author = {Mansfield, M.A. and Key, J.L.},
abstractNote = {Heat shock of living tissue induces the synthesis of a unique group of proteins, the heat shock proteins. In plants, the major group of heat shock proteins has a molecular mass of 15 to 25 kilodaltons. Accumulation to these proteins to stainable levels has been reported in only a few species. To examine accumulation of the low molecular weight heat shock proteins in a broader range of species, two-dimensional electrophoresis was used to resolve total protein from the following species: soybean (Glycine max L. Merr., var Wayne), pea (Pisum sativum L., var Early Alaska), sunflower (Helianthus annuus L.), wheat (Triticum asetivum L.), rice (Oryza sativa L., cv IR-36), maize (Zea mays L.), pearl millet (Pennisetum americanum L. Leeke, line 23DB), and Panicum miliaceum L. When identified by both silver staining and incorporation of radiolabel, a diverse array of low molecular weight heat shock proteins was synthesized in each of these species. These proteins accumulated to significant levels after three hours of heat shock but exhibited considerable heterogeneity in isoelectric point, molecular weight, stainability, and radiolabel incorporation. Although most appeared to be synthesized only during heat shock, some were detectable at low levels in control tissue. Compared to the monocots, a higher proportion of low molecular weight heat shock proteins was detectable in control tissues from dicots.},
doi = {10.1104/pp.84.4.1007},
journal = {Plant Physiology; (USA)},
number = ,
volume = 84:4,
place = {United States},
year = {Sat Aug 01 00:00:00 EDT 1987},
month = {Sat Aug 01 00:00:00 EDT 1987}
}